Cytosolic non-specific dipeptidase (CNDP2)

Cytosolic non-specific dipeptidase (CNDP2) is a metallopeptidase enzyme of the M20 family responsible for the hydrolysis of a broad range of dipeptides, particularly those containing hydrophobic amino acids, and has notable activity toward threonyl and some histidyl dipeptides, including carnosine[3][1][5]. CNDP2 can catalyze both peptide bond hydrolysis and, in reverse proteolysis, the formation of *N*-lactoyl-amino acids such as N-lactoyl-phenylalanine (Lac-Phe), which is implicated in energy metabolism after exercise and appetite regulation[4][3]. Expressed broadly in tissues such as liver, kidney, spleen, and brain, CNDP2 has been linked to metabolic regulation, oxidative stress defense (via glutathione metabolism), and various diseases including cancer (where it is often upregulated), diabetic nephropathy, cardiovascular disease, and neurodegenerative diseases like Parkinson’s disease[4][1]. CNDP2 is inhibited by bestatin and certain amino acid derivatives, but currently lacks approved drug modulators in clinical use[4]. Genetic variants of the *CNDP2* gene are associated with individual susceptibility to metabolic and renal diseases[4].

Other names

Carnosine dipeptidase 2CN2CPGLHEL-S-13PEPAFLJ10830HsT2298Glutamate carboxypeptidase-like protein 1Peptidase AThreonyl dipeptidaseCarnosinase-2Epididymis secretory protein Li 13

Enzyme inhibition (reduction of dipeptide/peptide hydrolysis), Potential metabolic modulation via blocking Lac-Phe formation, Modulation of oxidative stress handling